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Database: UniProt
Entry: C7RAG7_KANKD
LinkDB: C7RAG7_KANKD
Original site: C7RAG7_KANKD 
ID   C7RAG7_KANKD            Unreviewed;       950 AA.
AC   C7RAG7;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Kkor_0839 {ECO:0000313|EMBL:ACV26259.1};
OS   Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC   Kangiella.
OX   NCBI_TaxID=523791 {ECO:0000313|EMBL:ACV26259.1, ECO:0000313|Proteomes:UP000001231};
RN   [1] {ECO:0000313|EMBL:ACV26259.1, ECO:0000313|Proteomes:UP000001231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16069 / KCTC 12182 / SW-125
RC   {ECO:0000313|Proteomes:UP000001231};
RX   PubMed=21304661; DOI=10.4056/sigs.36635;
RA   Han C., Sikorski J., Lapidus A., Nolan M., Glavina Del Rio T., Tice H.,
RA   Cheng J.F., Lucas S., Chen F., Copeland A., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Bruce D., Goodwin L., Pitluck S., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Saunders E., Brettin T., Goker M., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Kangiella koreensis type strain (SW-125).";
RL   Stand. Genomic Sci. 1:226-233(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP001707; ACV26259.1; -; Genomic_DNA.
DR   RefSeq; WP_012800773.1; NC_013166.1.
DR   AlphaFoldDB; C7RAG7; -.
DR   STRING; 523791.Kkor_0839; -.
DR   KEGG; kko:Kkor_0839; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   eggNOG; COG4251; Bacteria.
DR   HOGENOM; CLU_000445_104_15_6; -.
DR   InParanoid; C7RAG7; -.
DR   OrthoDB; 9797243at2; -.
DR   Proteomes; UP000001231; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00088; HPT; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR019247; Histidine_kinase_BarA_N.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF09984; sCache_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACV26259.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001231};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACV26259.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          208..260
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          307..528
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          693..809
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          846..943
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   COILED          252..279
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         742
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         885
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   950 AA;  106153 MW;  A3AE342B2DEEA8E3 CRC64;
     MKEWGISKRI MTLALTPTIL VALLLGTLFI SNHINDSKYS LSARGKTIAT HLALASEYGL
     ITLDEKNLAE MAQAARDNDK DLMAVAIYDQ NNRVLASVGS AEMLSEMSFD NPYSLARSGS
     SNNLMRFART SDSEHGKLFY APIISKFPEN YESWQNYSQA NAQLLGYVAV MMTNEFSAIS
     RYNTILTTLF ITIIGLLIGG FLARRMSMSV TTPIEKMVEG INRIKDGHLD TRLESEASAE
     LLTLQEGINL MAENMEHNQE EMQLAVDQAT EDLRETLETL EVNNLELDIA RRQALEASRI
     KTEFLANMSH EIRTPMNGVI GFTELLLKTE LNNKQKDFLF DIKRSATSLL SIIDDILDYS
     KIEAGKMSFE RYPFDLRECV DDIFRMLGPN ANKKGIELVS LIYSDVPKAL LGDPIRIKQI
     ITNLVNNAIK FTKSGSVELY AEVESENQKG LKLKVQVKDS GIGLTQEQQR NLFKAFSQAD
     SSTKREFGGT GLGLVISKSL VEKMGGNIGV NSTAGDGSTF WFTLQCERTD SLPEDGLTGE
     FLANKSVLVF DPHPSTRLSI TQILEDWSML VRSFDKIDDL MTEIDLYSQS GKSIELIVIG
     GQRFRRRQQQ LEYICNKAQT QLLCPVITFS TAGNADFLEH LHSIGVSRAM TKPVTHRALY
     NSLIELLKTP LAASGKEPAP TVIGDASLLK NIYVLAVDDN PANLRLVTTL LQDLNIKVDA
     AESGMQAVSL SKNKVYDAIL MDIQMPEMDG LEATRTIRAN RTNLNTPIIA LTAHAMASER
     EQLLEAGMDD YMTKPVSEQA LINLLLKWTQ AASDLTPTEP EERKLDEAEQ DQTLDWSLSL
     KLANNNEQLA IDMLKMLVDS NFETGRNIHA AYQSQDFDQL LQHVHKLHGA SCYVGTPKLK
     HLSNVYETRL KKQQYNKLEE LHGELLAELE IINKEAERFL NPEEPETADN
//
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